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Yorodumi- PDB-2om2: Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif O... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2om2 | ||||||
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Title | Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif Of Rgs14 | ||||||
Components |
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Keywords | SIGNALING PROTEIN / Arginine finger / RGS14 GoLoco | ||||||
Function / homology | Function and homology information : / zygote asymmetric cell division / negative regulation of synaptic plasticity / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / GDP-dissociation inhibitor activity / GTPase activating protein binding / nucleocytoplasmic transport / positive regulation of neurogenesis / spindle organization ...: / zygote asymmetric cell division / negative regulation of synaptic plasticity / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / GDP-dissociation inhibitor activity / GTPase activating protein binding / nucleocytoplasmic transport / positive regulation of neurogenesis / spindle organization / platelet-derived growth factor receptor signaling pathway / Adenylate cyclase inhibitory pathway / positive regulation of protein localization to cell cortex / G-protein alpha-subunit binding / long-term memory / regulation of cAMP-mediated signaling / D2 dopamine receptor binding / G protein-coupled serotonin receptor binding / regulation of mitotic spindle organization / cellular response to forskolin / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / GTPase activator activity / negative regulation of MAP kinase activity / learning / long-term synaptic potentiation / Regulation of insulin secretion / G protein-coupled receptor binding / chromosome segregation / G-protein beta/gamma-subunit complex binding / visual learning / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / negative regulation of ERK1 and ERK2 cascade / ADP signalling through P2Y purinoceptor 12 / PML body / spindle / response to peptide hormone / Adrenaline,noradrenaline inhibits insulin secretion / G alpha (z) signalling events / spindle pole / ADORA2B mediated anti-inflammatory cytokines production / GPER1 signaling / GDP binding / heterotrimeric G-protein complex / signaling receptor complex adaptor activity / mitotic cell cycle / cell cortex / midbody / G alpha (i) signalling events / G alpha (s) signalling events / microtubule binding / response to oxidative stress / microtubule / dendritic spine / Extra-nuclear estrogen signaling / postsynaptic density / nuclear body / intracellular signal transduction / cell cycle / G protein-coupled receptor signaling pathway / cell division / lysosomal membrane / GTPase activity / centrosome / dendrite / glutamatergic synapse / GTP binding / nucleolus / protein kinase binding / magnesium ion binding / extracellular exosome / nucleoplasm / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Siderovski, D.P. / Kimple, R.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structure-based Protocol for Identifying Mutations that Enhance Protein-Protein Binding Affinities. Authors: Sammond, D.W. / Eletr, Z.M. / Purbeck, C. / Kimple, R.J. / Siderovski, D.P. / Kuhlman, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2om2.cif.gz | 163.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2om2.ent.gz | 125.6 KB | Display | PDB format |
PDBx/mmJSON format | 2om2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/om/2om2 ftp://data.pdbj.org/pub/pdb/validation_reports/om/2om2 | HTTPS FTP |
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-Related structure data
Related structure data | 1kjyS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 37159.348 Da / Num. of mol.: 2 / Fragment: G{alpha}i1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNAI1 / Plasmid: pPROEX Htb / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P63096 #2: Protein/peptide | Mass: 4093.621 Da / Num. of mol.: 2 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence occurs naturally in Homo sapiens (human). References: UniProt: Q506M1, UniProt: O43566*PLUS #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.26 Å3/Da / Density % sol: 62.21 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 1.55M Ammonium Sulfate, 100 mM Sodium Acetate pH 5.0, 10% Glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 18, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. all: 55498 / Num. obs: 55436 / % possible obs: 99.9 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1KJY Resolution: 2.2→20 Å / σ(F): 0
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Solvent computation | Bsol: 44.552 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.252 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Xplor file |
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